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Q1LCQ9 (ACDH2_RALME) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acetaldehyde dehydrogenase 2

EC=1.2.1.10
Alternative name(s):
Acetaldehyde dehydrogenase [acetylating] 2
Gene names
Ordered Locus Names:Rmet_5208
Encoded onPlasmid megaplasmid CH34
OrganismRalstonia metallidurans (strain CH34 / ATCC 43123 / DSM 2839) [Complete proteome] [HAMAP]
Taxonomic identifier266264 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus

Protein attributes

Sequence length314 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the conversion of acetaldehyde to acetyl-CoA, using NAD+ and coenzyme A. Is the final enzyme in the meta-cleavage pathway for the degradation of aromatic compounds By similarity. HAMAP-Rule MF_01657

Catalytic activity

Acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH. HAMAP-Rule MF_01657

Sequence similarities

Belongs to the acetaldehyde dehydrogenase family.

Ontologies

Keywords
   Biological processAromatic hydrocarbons catabolism
   LigandNAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
Plasmid
Gene Ontology (GO)
   Biological_processaromatic compound catabolic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functionNAD binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

acetaldehyde dehydrogenase (acetylating) activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 314314Acetaldehyde dehydrogenase 2 HAMAP-Rule MF_01657
PRO_0000387715

Regions

Nucleotide binding11 – 144NAD By similarity
Nucleotide binding160 – 1689NAD By similarity

Sites

Active site1291Acyl-thioester intermediate By similarity
Binding site2851NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1LCQ9 [UniParc].

Last modified May 30, 2006. Version 1.
Checksum: 074C27219B578DB8

FASTA31432,613
        10         20         30         40         50         60 
MKPCKVAIIG SGNIGTDLMI KILRHGKHVE MGAMVGIDPT SEGLARATRL GVPVTAAGID 

        70         80         90        100        110        120 
GLLAMPEFGE IRIAFDATSA GAHARHNATL QAHNVRVIDL TPAAIGPYVV PSVNAGEHLD 

       130        140        150        160        170        180 
APNLNMVTCG GQATIPIVAA VASVTPVHYA EIVASIASKS AGPGTRDNID EFTETTSRAI 

       190        200        210        220        230        240 
ESVGGARRGK AIIVLNPAEP PLIMRDTVCC LIDEADTAAI EAAVHAMVER MQGYVPGYRL 

       250        260        270        280        290        300 
KQRVQFDRID TPVNVPGLGP TTGLKVTVFL EVEGAAHYLP AYAGNLDIMT SAALACAERV 

       310 
AQALGNHHAL SAAS 

« Hide

References

[1]"Complete sequence of the megaplasmid of Ralstonia metallidurans CH34."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Martinez M., Goltsman E., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., Mergeay M., Benotmane M.A., Vallaeys T., Michaux A., Monchy S., Dunn J., McCorkle S., Taghavi S., van der Lelie D., Richardson P.
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CH34 / ATCC 43123 / DSM 2839.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000353 Genomic DNA. Translation: ABF12067.1.
RefSeqYP_587336.1. NC_007974.2.

3D structure databases

ProteinModelPortalQ1LCQ9.
SMRQ1LCQ9. Positions 5-306.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING266264.Rmet_5208.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABF12067; ABF12067; Rmet_5208.
GeneID4042069.
KEGGrme:Rmet_5208.
PATRIC20295176. VBIRalMet4734_5630.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG4569.
HOGENOMHOG000052149.
KOK04073.
OMAHARHEQL.
OrthoDBEOG6H1PXH.
ProtClustDBPRK08300.

Enzyme and pathway databases

BioCycCMET266264:GJ5G-5703-MONOMER.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
HAMAPMF_01657. Ac_ald_DH_ac.
InterProIPR003361. Acetaldehyde_dehydrogenase.
IPR015426. Acetylaldehyde_DH_C.
IPR016040. NAD(P)-bd_dom.
IPR000534. Semialdehyde_DH_NAD-bd.
[Graphical view]
PfamPF09290. AcetDehyd-dimer. 1 hit.
PF01118. Semialdhyde_dh. 1 hit.
[Graphical view]
PIRSFPIRSF015689. Actaldh_dh_actl. 1 hit.
SMARTSM00859. Semialdhyde_dh. 1 hit.
[Graphical view]
TIGRFAMsTIGR03215. ac_ald_DH_ac. 1 hit.
ProtoNetSearch...

Entry information

Entry nameACDH2_RALME
AccessionPrimary (citable) accession number: Q1LCQ9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 3, 2009
Last sequence update: May 30, 2006
Last modified: February 19, 2014
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families